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Collagen glycation

D.A. Slatter, N.C. Avery, A J. Bailey, Collagen in its Fibrillar State is Protected from Glycation, The International Journal of Biochemistry Cell Biology, 40(10), 2253 2263 (2008). [Pg.257]

Bailey AJ, Sims TJ, Avery NC and Halligan EP (1995) Non-enzymatic glycation of fibrous collagen reaction products of glucose and ribose. Biochem J 305, 385-390. [Pg.54]

Tian SF, Toda S, Higashimo H and Matsumara S (1996) Glycation decreases the stability of the triple-helical strands of fibrous collagen against proteolytic degradation by pepsin in a specific temperature range. J Biochem 120, 1153-1162. [Pg.55]

Odetti P, Pronzato MA, Noberasco G, Cosso L, Traverso N, Cottalasso D and Marinari UM (1994) Relationships between glycation and oxidation related fluorescences in rat collagen during aging. Lab Invest 70, 61-67. [Pg.71]

Wells-Knecht MG, Thorpe SR and Baynes JW (1995b) Pathways of formation of glycoxidation products during glycation of collagen. Biochemistry 34, 15134-15141. [Pg.71]

Deyl Z., Butenko G.M., Hausmann J. et al. (1990). Increased glycation and pigmentation of collagen in aged and young parabiotic rats and mice, Mech. Ageing Dev., 55, 39-47. [Pg.82]

Fig. 12.7. Analysis of Raman spectra obtained in vitro for Bruch s membrane, showing component spectra (a) and (b) for heme and collagen, respectively, and a residual spectrum (c) assigned to Raman responses of age-related glycation end products and proteins. Adapted from [29]... Fig. 12.7. Analysis of Raman spectra obtained in vitro for Bruch s membrane, showing component spectra (a) and (b) for heme and collagen, respectively, and a residual spectrum (c) assigned to Raman responses of age-related glycation end products and proteins. Adapted from [29]...
Diosmin, the 7-rutinoside of diosmetin, 3, 5,7-trihydroxy-4 -methoxyflavone, has been shown to decrease the formation of glycated collagen and haemoglobin in diabetic rats, as well as decreasing the formation of malondialdehyde.612... [Pg.168]

R. G. Paul, T. J. Sims, N. C. Avery, and A. J. Bailey, Identification and inhibition of glycation cross-links impairing the function of collagenous tissues, in F, 1998, 437. [Pg.192]

Activation of the polyol pathway results in a decrease of NADPH and NAD+ these are necessary cofactors in redox reactions throughout the body. The decreased concentration of these cofactors leads to decreased synthesis of reduced glutathione, nitric oxide, myoinositol and taurine. Myoinositol is particularly required for the normal function of nerves. Sorbitol may also glycate the amino nitrogen on proteins such as collagen, forming AGEs. [Pg.53]

Reiser KM (1991) Nonezymatic glycation of collagen in aging and diabetes. Proc Soc Exp Biol Med 196 17-29. [Pg.204]

Reiser KM, Amigable MA, Last JA (1992) Nonenzymatic glycation of the type I collagen. J Biol Chem 267 24207-24216. [Pg.204]

Aronson D. Cross-linking of glycated collagen in the pathogenesis of arterial and myocardial stiffening of aging and diabetes. J Hypertens 2003 21 3-12. [Pg.225]

K. lijima, M. Murata, H. Takahara, S. Me, and D. Fujimoto, Identification of iV -carboxymethylarginine as a novel acid-labile advanced glycation end product in collagen, Biochem. J., 347 (2000) 23-27. [Pg.392]

Herrmann, K.L., McCulloch, A.D., and Omens, J.H., Glycated collagen cross-linking alters cardiac mechanics in volume-overload hypertrophy. Am. J. Physiol Heart Circ. Physiol, 284, HI277—... [Pg.953]


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See also in sourсe #XX -- [ Pg.312 ]




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